7RSW

Crystal structure of group B human rotavirus VP8*

Summary for 7RSW

• Entry DOI: 10.2210/pdb7rsw/pdb
• Descriptor: Outer capsid protein VP4, peptide (3 entities in total)
• Functional Keywords: rotavirus, capsid, glycan-binding, structural protein
• Biological source: Rotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B, Rotavirus B (isolate adult diarrhea rotavirus)); More
• Total number of polymer chains: 3
• Total formula weight: 37496.04

Authors

Hu, L.,Salmen, W.,Sankaran, B.,Prasad, B.V. (deposition date: 2021-08-11, release date: 2022-07-20, Last modification date: 2024-05-22)

Primary citation

Hu, L.,Salmen, W.,Sankaran, B.,Lasanajak, Y.,Smith, D.F.,Crawford, S.E.,Estes, M.K.,Prasad, B.V.V.
Novel fold of rotavirus glycan-binding domain predicted by AlphaFold2 and determined by X-ray crystallography.
Commun Biol, 5:419-419, 2022

PubMed Abstract: The VP8* domain of spike protein VP4 in group A and C rotaviruses, which cause epidemic gastroenteritis in children, exhibits a conserved galectin-like fold for recognizing glycans during cell entry. In group B rotavirus, which causes significant diarrheal outbreaks in adults, the VP8* domain (VP8*B) surprisingly lacks sequence similarity with VP8* of group A or group C rotavirus. Here, by using the recently developed AlphaFold2 for ab initio structure prediction and validating the predicted model by determining a 1.3-Å crystal structure, we show that VP8*B exhibits a novel fold distinct from the galectin fold. This fold with a β-sheet clasping an α-helix represents a new fold for glycan recognition based on glycan array screening, which shows that VP8*B recognizes glycans containing N-acetyllactosamine moiety. Although uncommon, our study illustrates how evolution can incorporate structurally distinct folds with similar functionality in a homologous protein within the same virus genus.

PubMed: 35513489
DOI: 10.1038/s42003-022-03357-1

Experimental method

X-RAY DIFFRACTION (1.32 Å)